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  • 1
    Electronic Resource
    Electronic Resource
    Cytochromes of the non-thiosulfate-utilizing green sulfur bacterium Chlorobium limicola (1981)
    Springer
    Archives of microbiology 130 (1981), S. 31-37 
    Details
    ISSN: 1432-072X
    Keywords: Chlorobium limicola ; Flavocytochrome c-553 ; Cytochrome c-555 ; Rubredoxin ; Sulfur metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Flavocytochrome c-553 of the non-thiosulfateutilizing green sulfur bacterium Chlorobium limicola strain 6330 was partially purified by ion exchange column chromatography and ammonium sulfate fractionation (highest purity index obtained: A 280/A 417 red=0.96). It is autoxidizable and located in the soluble fraction. This hemoprotein contains a flavin component and one heme per molecule. The dithionite reduced spectrum reveals the typical maxima of a c-type cytochrome: α=553,5 nm; β=523 nm; γ=417 nm, while the oxidized form shows a γ-band at 410 nm and two shoulders at 440 nm and 480 nm indicating the flavin component. The flavocytochrome is a basic protein with an isoelectric point at pH 9.0 (± 0.5), a redox potential of 65 mV, a molecular weight of 56,000. It participates in sulfide oxidation and shows neither adenylylsulfate reductase nor sulfite reductase activity. C. limicola further contains a soluble cytochrome c-555 (highest purity index obtained: A 280/A 412 ox=0.13; isoelectric point between pH 9.5 and 10) and the non-heme iron-containing proteins rubredoxin and ferredoxin, but lacks cytochrome c-551. Besides these soluble electron transfer proteins a membrane-bound c-type cytochrome (α=554,5 nm) can be detected spectrophotometrically.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00527068
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  • 2
    Electronic Resource
    Electronic Resource
    Cytochrome c-555 and iron-sulfur-proteins of the non-thiosulfate-utilizing green sulfur bacterium Chlorobium vibrioforme (1983)
    Springer
    Archives of microbiology 135 (1983), S. 186-190 
    Details
    ISSN: 1432-072X
    Keywords: Chlorobium vibrioforme ; Cytochrome c-555 ; Rubredoxins ; Ferredoxin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The non-thiosulfate-utilizing green sulfur bacterium Chlorobium vibrioforme contains only one soluble c-type cytochrome (c-555) besides two rubredoxins and ferredoxin. These electron transfer proteins were highly purified by ion exchange chromatography and gel filtration. Cytochrome c-555 is a small and weakly basic hemoprotein with an isoelectric point at pH 7.3, a redoxpotential of + 80 mV, and a molecular weight of 11,500 (±500) determined by electrophoresis on sodium dodecylsulfate polyacrylamide gel, and of 11,000 by gel filtration on Sephadex G-75. Cytochrome c-555 shows maxima at 412.5 nm in the oxidized form, and three maxima in the reduced state (α-band at 555 nm with a shoulder at 551 nm, β-band at 523 nm, and γ-band at 418 nm). The best purity index (A280/A418) obtained was 0.15. The two rubredoxins (rub I and rub II) are acidic small proteins and both have the same molecular weight of 8,100 estimated by gel filtration on Sephadex G-75 and show the same maxima at 370 nm, 492 nm, and 575 nm in the oxidized form but differ only in their isoelectric points at pH 2.9 (rub I) and at pH 2.7 (rub II). The best purity index obtained (A280/A370) was 3.27 for rub I and 3.57 for rub II respectively. Both rubredoxins contain one iron atom per molecule. Ferredoxin is also an acidic protein with an isoelectric point at pH 2.5 and shows maxima at 300 nm and 380 nm in the oxidized form.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414477
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  • 3
    Electronic Resource
    Electronic Resource
    Cytochromes of the green sulfur bacterium Chlorobium vibrioforme f. thiosulfatophilum. Purification, characterization and sulfur metabolism (1982)
    Springer
    Archives of microbiology 131 (1982), S. 19-26 
    Details
    ISSN: 1432-072X
    Keywords: Chlorobium vibrioforme f. thiosulfatophilum ; Cytochrome c-551 ; Flavocytochrome c-553 ; Cytochrome c-555 ; Sulfur metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Three cytochromes of the thiosulfate-utilizing green sulfur bacterium Chlorobium vibrioforme f. thiosulfatophilum were highly purified by ion exchange column chromatography and ammonium sulfate fractionation. All three cytochromes are located in the soluble fraction. Cytochrome c-551 (highest purity index obtained: A280/A416=0.39) shows maxima at 551 nm (α-band), 521 nm (β-band), and 416 nm (γ-band) for the reduced form. This cytochrome is an acidic protein with a molecular weight of 32,000, a redox potential of 150 mV, and an isoelectric point at pH 6.0. Cytochrome c-553 (highest purity index obtained: A280/A417=0.8) is also an acidic protein with maxima at 553,5 nm, 523,5 nm and 417 nm for the reduced form, a molecular weight of 63,000, a redox potential of 90 mV, an isoelectric point at pH 6.3, and it contains FAD as flavin component. It is autoxidizable and participates in sulfide oxidation, but cannot catalyze the reverse reaction. The cytochrome c-555 (highest purity index obtained: A280/A418=0.16) is a small basic protein with maxima at 555 nm, 523 nm and 418 nm (reduced form), a molecular weight of 12,500, an isoelectric point between pH 10 and 10.5, and a redox potential of 155 mV. The ratio of the cytochrome contents to each other is constant and does not change when the organism has only thiosulfate or sulfide as the main electron donor in the medium. The soluble fraction further contains the non-heme ironcontaining proteins rubredoxin and ferredoxin. The anaerobic sulfide oxidation in a growing culture of Chlorobium vibrioforme f. thiosulfatophilum is accompanied by a rapid formation of thiosulfate, which is only utilized when sulfide is no longer available, while the elemental sulfur concentration increases constantly until thiosulfate is consumed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00451493
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  • 4
    Electronic Resource
    Electronic Resource
    Cytochromes, rubredoxin, and sulfur metabolism of the non-thiosulfate-utilizing green sulfur bacterium Pelodictyon luteolum (1982)
    Springer
    Archives of microbiology 132 (1982), S. 204-210 
    Details
    ISSN: 1432-072X
    Keywords: Pelodictyon luteolum ; Cytochrome c-553 ; Cytochrome c-555 ; Rubredoxin ; Anaerobic sulfide oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two soluble c-type cytochromes (c-553 and c-555) and the nonheme iron-containing protein rubredoxin of the non-thiosulfate-utilizing green sulfur bacterium Pelodictyon luteolum were highly purified by ion exchange column chromatography, gel filtration and ammonium sulfate fractionation. Both cytochrome are small and basic hemoproteins, while rubredoxin is an acidic small nonheme iron protein. Cytochrome c-553 has a molecular weight of 13,000 determined by Sephacryl S-200 chromatography and of 10,700 by electrophoresis on SDS acrylamide gel, an isoelectric point at pH 10.2, a redox-potential of +220 mV. It shows maxima at 413 nm in the oxidized form, and the characteristic three maxima in the reduced state (α-band at 553 nm, β-band at 523 nm, γ-band at 417 nm). The best purity index (A 280/A 417) obtained was 0.18. Cytochrome c-555 (best purity index obtained: A 280/A 418=0.17) has an isoelectric point at pH 10.5, a molecular weight of 9,500 (by electrophoresis on SDS acrylamide gel) and a redox-potential of +160mV. The reduced form of this cytochrome shows the typical bands of c-type cytochromes at 555 (551) nm (α-band), 523 nm (β-band) and 418 nm (γ-band), while the oxidized form has the γ-band at 413 nm. Rubredoxin (best purity index obtained: A 280/A 490=3.5) is an acidic small protein. Its molecular weight estimated by gel filtration and SDS acrylamide gel electrophoresis is 27,000 and 6,300 respectively. The monomer of this protein contains one iron atom per molecule. Rubredoxin has an isoelectric point at pH 2.8 and shows maxima at 570 nm, 490 nm and 370 nm in the oxidized form. During anaerobic sulfide oxidation of a growing culture of Pelodictyon luteolum elemental sulfur is the first main product, which appears in the medium. Elemental sulfur is further oxidized to sulfate, after the available sulfide is completely consumed by the cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00508732
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  • 5
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    The dynamic genome of Hydra (2010)
    Nature Publishing Group (NPG)
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    Publication Date: 2010-03-17
    Description: The freshwater cnidarian Hydra was first described in 1702 and has been the object of study for 300 years. Experimental studies of Hydra between 1736 and 1744 culminated in the discovery of asexual reproduction of an animal by budding, the first description of regeneration in an animal, and successful transplantation of tissue between animals. Today, Hydra is an important model for studies of axial patterning, stem cell biology and regeneration. Here we report the genome of Hydra magnipapillata and compare it to the genomes of the anthozoan Nematostella vectensis and other animals. The Hydra genome has been shaped by bursts of transposable element expansion, horizontal gene transfer, trans-splicing, and simplification of gene structure and gene content that parallel simplification of the Hydra life cycle. We also report the sequence of the genome of a novel bacterium stably associated with H. magnipapillata. Comparisons of the Hydra genome to the genomes of other animals shed light on the evolution of epithelia, contractile tissues, developmentally regulated transcription factors, the Spemann-Mangold organizer, pluripotency genes and the neuromuscular junction.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4479502/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4479502/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chapman, Jarrod A -- Kirkness, Ewen F -- Simakov, Oleg -- Hampson, Steven E -- Mitros, Therese -- Weinmaier, Thomas -- Rattei, Thomas -- Balasubramanian, Prakash G -- Borman, Jon -- Busam, Dana -- Disbennett, Kathryn -- Pfannkoch, Cynthia -- Sumin, Nadezhda -- Sutton, Granger G -- Viswanathan, Lakshmi Devi -- Walenz, Brian -- Goodstein, David M -- Hellsten, Uffe -- Kawashima, Takeshi -- Prochnik, Simon E -- Putnam, Nicholas H -- Shu, Shengquiang -- Blumberg, Bruce -- Dana, Catherine E -- Gee, Lydia -- Kibler, Dennis F -- Law, Lee -- Lindgens, Dirk -- Martinez, Daniel E -- Peng, Jisong -- Wigge, Philip A -- Bertulat, Bianca -- Guder, Corina -- Nakamura, Yukio -- Ozbek, Suat -- Watanabe, Hiroshi -- Khalturin, Konstantin -- Hemmrich, Georg -- Franke, Andre -- Augustin, Rene -- Fraune, Sebastian -- Hayakawa, Eisuke -- Hayakawa, Shiho -- Hirose, Mamiko -- Hwang, Jung Shan -- Ikeo, Kazuho -- Nishimiya-Fujisawa, Chiemi -- Ogura, Atshushi -- Takahashi, Toshio -- Steinmetz, Patrick R H -- Zhang, Xiaoming -- Aufschnaiter, Roland -- Eder, Marie-Kristin -- Gorny, Anne-Kathrin -- Salvenmoser, Willi -- Heimberg, Alysha M -- Wheeler, Benjamin M -- Peterson, Kevin J -- Bottger, Angelika -- Tischler, Patrick -- Wolf, Alexander -- Gojobori, Takashi -- Remington, Karin A -- Strausberg, Robert L -- Venter, J Craig -- Technau, Ulrich -- Hobmayer, Bert -- Bosch, Thomas C G -- Holstein, Thomas W -- Fujisawa, Toshitaka -- Bode, Hans R -- David, Charles N -- Rokhsar, Daniel S -- Steele, Robert E -- P 21108/Austrian Science Fund FWF/Austria -- R24 RR015088/RR/NCRR NIH HHS/ -- England -- Nature. 2010 Mar 25;464(7288):592-6. doi: 10.1038/nature08830. Epub 2010 Mar 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉US Department of Energy Joint Genome Institute, Walnut Creek, California 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20228792" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa/genetics ; Comamonadaceae/genetics ; DNA Transposable Elements/genetics ; Gene Transfer, Horizontal/genetics ; Genome/*genetics ; Genome, Bacterial/genetics ; Hydra/*genetics/microbiology/ultrastructure ; Molecular Sequence Data ; Neuromuscular Junction/ultrastructure
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 6
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    Molecular mechanism of action of microtubule-stabilizing anticancer agents (2013)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2013-01-05
    Description: Microtubule-stabilizing agents (MSAs) are efficacious chemotherapeutic drugs widely used for the treatment of cancer. Despite the importance of MSAs for medical applications and basic research, their molecular mechanisms of action on tubulin and microtubules remain elusive. We determined high-resolution crystal structures of alphabeta-tubulin in complex with two unrelated MSAs, zampanolide and epothilone A. Both compounds were bound to the taxane pocket of beta-tubulin and used their respective side chains to induce structuring of the M-loop into a short helix. Because the M-loop establishes lateral tubulin contacts in microtubules, these findings explain how taxane-site MSAs promote microtubule assembly and stability. Further, our results offer fundamental structural insights into the control mechanisms of microtubule dynamics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prota, Andrea E -- Bargsten, Katja -- Zurwerra, Didier -- Field, Jessica J -- Diaz, Jose Fernando -- Altmann, Karl-Heinz -- Steinmetz, Michel O -- New York, N.Y. -- Science. 2013 Feb 1;339(6119):587-90. doi: 10.1126/science.1230582. Epub 2013 Jan 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomolecular Research, Paul Scherrer Institut, Villigen PSI, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23287720" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/*chemistry/pharmacology ; Binding Sites ; Bridged Compounds/chemistry/pharmacology ; Cattle ; Chickens ; Crystallography, X-Ray ; Epothilones/*chemistry/pharmacology ; Macrolides/*chemistry/pharmacology ; Microtubules/*drug effects ; Protein Structure, Secondary ; Taxoids/chemistry/pharmacology ; Tubulin/*chemistry ; Tubulin Modulators/*chemistry/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Visual space is compressed in prefrontal cortex before eye movements (2014)
    Nature Publishing Group (NPG)
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    Publication Date: 2014-03-29
    Description: We experience the visual world through a series of saccadic eye movements, each one shifting our gaze to bring objects of interest to the fovea for further processing. Although such movements lead to frequent and substantial displacements of the retinal image, these displacements go unnoticed. It is widely assumed that a primary mechanism underlying this apparent stability is an anticipatory shifting of visual receptive fields (RFs) from their presaccadic to their postsaccadic locations before movement onset. Evidence of this predictive 'remapping' of RFs has been particularly apparent within brain structures involved in gaze control. However, critically absent among that evidence are detailed measurements of visual RFs before movement onset. Here we show that during saccade preparation, rather than remap, RFs of neurons in a prefrontal gaze control area massively converge towards the saccadic target. We mapped the visual RFs of prefrontal neurons during stable fixation and immediately before the onset of eye movements, using multi-electrode recordings in monkeys. Following movements from an initial fixation point to a target, RFs remained stationary in retinocentric space. However, in the period immediately before movement onset, RFs shifted by as much as 18 degrees of visual angle, and converged towards the target location. This convergence resulted in a threefold increase in the proportion of RFs responding to stimuli near the target region. In addition, like in human observers, the population of prefrontal neurons grossly mislocalized presaccadic stimuli as being closer to the target. Our results show that RF shifts do not predict the retinal displacements due to saccades, but instead reflect the overriding perception of target space during eye movements.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4064801/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4064801/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zirnsak, Marc -- Steinmetz, Nicholas A -- Noudoost, Behrad -- Xu, Kitty Z -- Moore, Tirin -- EY014924/EY/NEI NIH HHS/ -- R01 EY014924/EY/NEI NIH HHS/ -- T32 MH020016/MH/NIMH NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2014 Mar 27;507(7493):504-7. doi: 10.1038/nature13149.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Department of Neurobiology, Stanford University School of Medicine, Stanford, California 94305, USA [2] Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305, USA. ; Department of Neurobiology, Stanford University School of Medicine, Stanford, California 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24670771" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Electrodes ; Fixation, Ocular/physiology ; Humans ; Macaca mulatta ; Male ; Models, Neurological ; Neurons/physiology ; Prefrontal Cortex/cytology/*physiology ; Retina/physiology ; Saccades/*physiology ; Visual Acuity/physiology ; Visual Fields/physiology ; Visual Perception/*physiology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 8
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    Independent evolution of striated muscles in cnidarians and bilaterians (2012)
    Nature Publishing Group (NPG)
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    Publication Date: 2012-07-06
    Description: Striated muscles are present in bilaterian animals (for example, vertebrates, insects and annelids) and some non-bilaterian eumetazoans (that is, cnidarians and ctenophores). The considerable ultrastructural similarity of striated muscles between these animal groups is thought to reflect a common evolutionary origin. Here we show that a muscle protein core set, including a type II myosin heavy chain (MyHC) motor protein characteristic of striated muscles in vertebrates, was already present in unicellular organisms before the origin of multicellular animals. Furthermore, 'striated muscle' and 'non-muscle' myhc orthologues are expressed differentially in two sponges, compatible with a functional diversification before the origin of true muscles and the subsequent use of striated muscle MyHC in fast-contracting smooth and striated muscle. Cnidarians and ctenophores possess striated muscle myhc orthologues but lack crucial components of bilaterian striated muscles, such as genes that code for titin and the troponin complex, suggesting the convergent evolution of striated muscles. Consistently, jellyfish orthologues of a shared set of bilaterian Z-disc proteins are not associated with striated muscles, but are instead expressed elsewhere or ubiquitously. The independent evolution of eumetazoan striated muscles through the addition of new proteins to a pre-existing, ancestral contractile apparatus may serve as a model for the evolution of complex animal cell types.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3398149/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3398149/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steinmetz, Patrick R H -- Kraus, Johanna E M -- Larroux, Claire -- Hammel, Jorg U -- Amon-Hassenzahl, Annette -- Houliston, Evelyn -- Worheide, Gert -- Nickel, Michael -- Degnan, Bernard M -- Technau, Ulrich -- P 21108/Austrian Science Fund FWF/Austria -- England -- Nature. 2012 Jul 12;487(7406):231-4. doi: 10.1038/nature11180.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department for Molecular Evolution and Development, Centre for Organismal Systems Biology, University of Vienna, A-1090 Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22763458" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Cnidaria/*anatomy & histology/genetics/metabolism ; Gene Duplication ; Gene Expression Regulation ; Muscle, Striated/metabolism/*physiology ; Myosin Heavy Chains/genetics/metabolism ; Phylogeny
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
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    Protection against atherogenesis in mice mediated by human apolipoprotein A-IV (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-16
    Description: Apolipoproteins are protein constituents of plasma lipid transport particles. Human apolipoprotein A-IV (apoA-IV) was expressed in the liver of C57BL/6 mice and mice deficient in apoE, both of which are prone to atherosclerosis, to investigate whether apoA-IV protects against this disease. In transgenic C57BL/6 mice on an atherogenic diet, the serum concentration of high density lipoprotein (HDL) cholesterol increased by 35 percent, whereas the concentration of endogenous apoA-I decreased by 29 percent, relative to those in transgenic mice on a normal diet. Expression of human apoA-IV in apoE-deficient mice on a normal diet resulted in an even more severe atherogenic lipoprotein profile, without affecting the concentration of HDL cholesterol, than that in nontransgenic apoE-deficient mice. However, transgenic mice of both backgrounds showed a substantial reduction in the size of atherosclerotic lesions. Thus, apoA-IV appears to protect against atherosclerosis by a mechanism that does not involve an increase in HDL cholesterol concentration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duverger, N -- Tremp, G -- Caillaud, J M -- Emmanuel, F -- Castro, G -- Fruchart, J C -- Steinmetz, A -- Denefle, P -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):966-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rhone-Poulenc Rorer, Gencell Division, Atherosclerosis Department, Centre de Recherches de Vitry-Alfortville, 94403 Vitry sur Seine Cedex, France. G. C.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688083" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apolipoprotein A-I/blood ; Apolipoproteins A/blood/*physiology ; Apolipoproteins E/blood/deficiency ; Arteriosclerosis/*prevention & control ; Cholesterol/blood ; Cholesterol, HDL/blood ; Diet, Atherogenic ; Female ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Dissecting the genetic basis of resistance to malaria parasites in Anopheles gambiae (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-03
    Description: The ability of Anopheles gambiae mosquitoes to transmit Plasmodium parasites is highly variable between individuals. However, the genetic basis of this variability has remained unknown. We combined genome-wide mapping and reciprocal allele-specific RNA interference (rasRNAi) to identify the genomic locus that confers resistance to malaria parasites and demonstrated that polymorphisms in a single gene encoding the antiparasitic thioester-containing protein 1 (TEP1) explain a substantial part of the variability in parasite killing. The link between TEP1 alleles and resistance to malaria may offer new tools for controlling malaria transmission. The successful application of rasRNAi in Anopheles suggests that it could also be applied to other organisms where RNAi is feasible to dissect complex phenotypes to the level of individual quantitative trait alleles.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2959166/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2959166/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blandin, Stephanie A -- Wang-Sattler, Rui -- Lamacchia, Marina -- Gagneur, Julien -- Lycett, Gareth -- Ning, Ye -- Levashina, Elena A -- Steinmetz, Lars M -- R01 GM068717/GM/NIGMS NIH HHS/ -- R01 GM068717-08/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Oct 2;326(5949):147-50. doi: 10.1126/science.1175241.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19797663" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Anopheles gambiae/*genetics/immunology/metabolism/*parasitology ; Chromosome Mapping ; *Genes, Insect ; Genome, Insect ; Immunity, Innate ; Insect Proteins/*genetics/*metabolism ; Insect Vectors/genetics/immunology/metabolism/parasitology ; Mice ; Models, Molecular ; Molecular Sequence Data ; Phenotype ; Plasmodium berghei/immunology/*physiology ; *Polymorphism, Genetic ; Quantitative Trait Loci ; RNA Interference
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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